ID A0A1J4VAP3_9BACT Unreviewed; 382 AA.
AC A0A1J4VAP3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AUJ70_01545 {ECO:0000313|EMBL:OIO34242.1};
OS Candidatus Omnitrophica bacterium CG1_02_40_15.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1805284 {ECO:0000313|EMBL:OIO34242.1, ECO:0000313|Proteomes:UP000183570};
RN [1] {ECO:0000313|EMBL:OIO34242.1, ECO:0000313|Proteomes:UP000183570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_40_15 {ECO:0000313|EMBL:OIO34242.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIO34242.1}.
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DR EMBL; MNVP01000029; OIO34242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4VAP3; -.
DR STRING; 1805284.AUJ70_01545; -.
DR Proteomes; UP000183570; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 168..382
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 134..161
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 382 AA; 42704 MW; 901837D2A80B0973 CRC64;
MDEQVIKVLI VDFNSANISK INDALSSMPG ISYDISWLQS EENVLKKVEE EKFDIILLSY
DISGLNGLEI LSGLQYKELS GPIIMMADAE DKEFAPQAMR EGAYDYVIRE KGFEKGLPVI
MHNAMAAFYA AKERERLQKE IAAKKIELEA ANRKLQQLDK IKSDFVANVA HEFRTPLMII
KGNVDLVNKG GLGSVAPAQK EMLDGAINIV NRLSRLVNDL LDISKIESGK MELKKEPVQM
NNIIEENLAV FDKIIKDKKQ RLEKDLAMDL SEISADKDKV AQIFVNLLSN AIKYTPQSGT
ITIKTVNLEK EIMVEISDTG EGVAPDSLDK IFDKFTRVTT EKKEGTGLGL PIAKDIVNLH
NGRIWVKSEL GKGSHFYFTL PK
//